Unknown

Dataset Information

0

Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein.


ABSTRACT: A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus (RVFV) L protein using a combination of in silico techniques. Due to its large size and multiple domains, elucidation of the tertiary structure of the L protein has so far challenged both dry and wet laboratories. In this work, we leverage complementary perspectives and tools from the computational-molecular-biology and bioinformatics domains for constructing, refining, and evaluating several atomistic structural models of the L protein that are physically realistic. All computed models have very flexible termini of about 200 amino acids each, and a high proportion of helical regions. Properties such as potential energy, radius of gyration, hydrodynamics radius, flexibility coefficient, and solvent-accessible surface are reported. Structural characterization of the L protein enables our laboratories to better understand viral replication and transcription via further studies of L protein-mediated protein-protein interactions. While results presented a focus on the RVFV L protein, the following workflow is a more general modeling protocol for discovering the tertiary structure of multidomain proteins consisting of thousands of amino acids.

SUBMITTER: Gogovi GK 

PROVIDER: S-EPMC6539450 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Modeling the Tertiary Structure of the Rift Valley Fever Virus L Protein.

Gogovi Gideon K GK   Almsned Fahad F   Bracci Nicole N   Kehn-Hall Kylene K   Shehu Amarda A   Blaisten-Barojas Estela E  

Molecules (Basel, Switzerland) 20190507 9


A tertiary structure governs, to a great extent, the biological activity of a protein in the living cell and is consequently a central focus of numerous studies aiming to shed light on cellular processes central to human health. Here, we aim to elucidate the structure of the Rift Valley fever virus (RVFV) L protein using a combination of in silico techniques. Due to its large size and multiple domains, elucidation of the tertiary structure of the L protein has so far challenged both dry and wet  ...[more]

Similar Datasets

| PRJNA517473 | ENA
| PRJNA518058 | ENA
| S-EPMC3828160 | biostudies-literature
| S-EPMC8826900 | biostudies-literature
| S-EPMC3562824 | biostudies-literature
| S-EPMC6555543 | biostudies-literature
| S-EPMC4906348 | biostudies-other
| S-EPMC8877469 | biostudies-literature
| S-EPMC2900692 | biostudies-literature
| S-EPMC3311189 | biostudies-literature